Evidence map›Paper›PMID 18079695›Full record

ArticleThe EMBO journal2008

Real-time detection reveals that effectors couple dynamin's GTP-dependent conformational changes to the membrane.

Rajesh Ramachandran, Sandra L Schmid

Open access · bronzeAbstract readValidation Study
In one paragraph

Article in The EMBO journal, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 59 papers.

0numbers the graph read from it
0cells of the map it votes in
59citing papers in PubMed
4.6field-weighted citation impact, top 4% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

59 citing papers in PubMed, 107 citations in OpenAlex.

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  20. Endocytic proteins drive vesicle growth via instability in high membrane tension environment.Proceedings of the National Academy of Sciences of the United States of America · 2015
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

2 authors at 1 institution in 1 country.

Rajesh RamachandranDepartment of Cell Biology, The Scripps Research Institute, La Jolla, CA 92037, USA.
Sandra L Schmid
Scripps Research Institute · US

Funding

EARLY STEPS IN RECEPTOR-MEDIATED ENDOCYTOSISR01GM042455 · NIGMS · UT SOUTHWESTERN MEDICAL CENTER · PI METTLEN, MARCEL BERNARD · 1989 to 2020
$8.2M
The Clathrin Coated Vesicle CycleR01MH061345 · NIMH · UT SOUTHWESTERN MEDICAL CENTER · PI SCHMID, SANDRA L. · 2010 to 2019
$5.0M
THE CLATHRIN COATED VESICLE CYCLER37MH061345 · NIMH · SCRIPPS RESEARCH INSTITUTE, THE · PI SCHMID, SANDRA L. · 2000 to 2009
$4.7M
NIGMS NIH HHS R01 GM042455NIGMS NIH HHS R01.GM42455NIMH NIH HHS R01 MH061345NIMH NIH HHS R37 MH061345NIMH NIH HHS R37.MH61345
6 · The paper itself

Abstract

The GTPase dynamin is a mechanochemical enzyme involved in membrane fission, but the molecular nature of its membrane interactions and their regulation by guanine nucleotides and protein effectors remain poorly characterized. Using site-directed fluorescence labeling and several independent fluorescence spectroscopic techniques, we have developed robust assays for the detection and real-time monitoring of dynamin-membrane and dynamin-dynamin interactions. We show that dynamin interacts preferentially with highly curved, PIP2-dense membranes and inserts partially into the lipid bilayer. Our kinetic measurements further reveal that cycles of GTP binding and hydrolysis elicit major conformational rearrangements in self-assembled dynamin that favor dynamin-membrane association and dissociation, respectively. Sorting nexin 9, an abundant dynamin partner, transiently stabilizes dynamin on the membrane at the onset of stimulated GTP hydrolysis and may function to couple dynamin's mechanochemical conformational changes to membrane destabilization. Amphiphysin I has the opposite effect. Thus, dynamin's mechanochemical properties on a membrane surface are dynamically regulated by its GTPase cycle and major binding partners.

Indexed as

AnimalsCell MembraneCells, CulturedDynamin IGuanosine TriphosphateHumansInsectaLipid BilayersLiposomesMutagenesis, Site-DirectedPhosphatidylcholinesPhosphatidylinositol 4,5-DiphosphateProtein ConformationSpectrometry, FluorescenceSwine1,2-oleoylphosphatidylcholineDynamin IGuanosine TriphosphateLipid BilayersLiposomesPhosphatidylcholinesPhosphatidylinositol 4,5-Diphosphate

Identifiers

PMID18079695
PMCPMC2206142
OpenAlexW2134302470

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.